TBCE_MOUSE
ID TBCE_MOUSE Reviewed; 524 AA.
AC Q8CIV8;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Tubulin-specific chaperone E;
DE AltName: Full=Tubulin-folding cofactor E;
GN Name=Tbce;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS
RP VAL-348 AND GLY-524.
RC STRAIN=129S2/SvPas;
RX PubMed=12389029; DOI=10.1038/ng1016;
RA Martin N., Jaubert J., Gounon P., Salido E., Haase G., Szatanik M.,
RA Guenet J.-L.;
RT "A missense mutation in Tbce causes progressive motor neuronopathy in
RT mice.";
RL Nat. Genet. 32:443-447(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129/Sv X 129/SvCp; TISSUE=Embryonic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH TBCB.
RX PubMed=17184771; DOI=10.1016/j.yexcr.2006.09.002;
RA Kortazar D., Fanarraga M.L., Carranza G., Bellido J., Villegas J.C.,
RA Avila J., Zabala J.C.;
RT "Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer
RT dissociation.";
RL Exp. Cell Res. 313:425-436(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR OF 441-524.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal ubiquitin-like domain.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tubulin-folding protein; involved in the second step of the
CC tubulin folding pathway and in the regulation of tubulin heterodimer
CC dissociation (PubMed:12389029, PubMed:17184771). Required for correct
CC organization of microtubule cytoskeleton and mitotic splindle, and
CC maintenance of the neuronal microtubule network (By similarity).
CC {ECO:0000250|UniProtKB:Q15813, ECO:0000269|PubMed:12389029,
CC ECO:0000269|PubMed:17184771}.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state. Cofactors B and E
CC can form a heterodimer which binds to alpha-tubulin and enhances their
CC ability to dissociate tubulin heterodimers. Interacts with TBCD (By
CC similarity). {ECO:0000250|UniProtKB:Q15813,
CC ECO:0000269|PubMed:17184771}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12389029}.
CC -!- SIMILARITY: Belongs to the TBCE family. {ECO:0000305}.
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DR EMBL; AY082332; AAL92570.1; -; mRNA.
DR EMBL; AK167383; BAE39475.1; -; mRNA.
DR EMBL; BC050206; AAH50206.1; -; mRNA.
DR CCDS; CCDS26247.1; -.
DR RefSeq; NP_848027.1; NM_178337.3.
DR PDB; 1WJN; NMR; -; A=441-524.
DR PDBsum; 1WJN; -.
DR AlphaFoldDB; Q8CIV8; -.
DR BMRB; Q8CIV8; -.
DR SMR; Q8CIV8; -.
DR BioGRID; 214045; 6.
DR STRING; 10090.ENSMUSP00000047880; -.
DR PhosphoSitePlus; Q8CIV8; -.
DR EPD; Q8CIV8; -.
DR MaxQB; Q8CIV8; -.
DR PaxDb; Q8CIV8; -.
DR PeptideAtlas; Q8CIV8; -.
DR PRIDE; Q8CIV8; -.
DR ProteomicsDB; 263136; -.
DR DNASU; 70430; -.
DR Ensembl; ENSMUST00000039894; ENSMUSP00000047880; ENSMUSG00000039233.
DR GeneID; 70430; -.
DR KEGG; mmu:70430; -.
DR UCSC; uc007pmq.2; mouse.
DR CTD; 6905; -.
DR MGI; MGI:1917680; Tbce.
DR VEuPathDB; HostDB:ENSMUSG00000039233; -.
DR eggNOG; KOG3207; Eukaryota.
DR GeneTree; ENSGT00530000063405; -.
DR HOGENOM; CLU_017716_5_0_1; -.
DR InParanoid; Q8CIV8; -.
DR OMA; KKYALDW; -.
DR OrthoDB; 249920at2759; -.
DR PhylomeDB; Q8CIV8; -.
DR TreeFam; TF313455; -.
DR BioGRID-ORCS; 70430; 21 hits in 58 CRISPR screens.
DR ChiTaRS; Tbce; mouse.
DR EvolutionaryTrace; Q8CIV8; -.
DR PRO; PR:Q8CIV8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8CIV8; protein.
DR Bgee; ENSMUSG00000039233; Expressed in retinal neural layer and 272 other tissues.
DR ExpressionAtlas; Q8CIV8; baseline and differential.
DR Genevisible; Q8CIV8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; TAS:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0014889; P:muscle atrophy; IMP:MGI.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IMP:MGI.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006457; P:protein folding; TAS:MGI.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR CDD; cd17044; Ubl_TBCE; 1.
DR Gene3D; 2.30.30.190; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044079; Ubl_TBCE.
DR PANTHER; PTHR15140; PTHR15140; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Cytoskeleton;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT CHAIN 2..524
FT /note="Tubulin-specific chaperone E"
FT /id="PRO_0000083539"
FT DOMAIN 27..71
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REPEAT 154..175
FT /note="LRR 1"
FT REPEAT 180..201
FT /note="LRR 2"
FT REPEAT 206..227
FT /note="LRR 3"
FT REPEAT 231..253
FT /note="LRR 4"
FT REPEAT 254..275
FT /note="LRR 5"
FT REPEAT 279..300
FT /note="LRR 6"
FT REPEAT 309..330
FT /note="LRR 7"
FT DOMAIN 343..381
FT /note="LRRCT"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT MOD_RES 460
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT VARIANT 348
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:12389029"
FT VARIANT 524
FT /note="W -> G"
FT /evidence="ECO:0000269|PubMed:12389029"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:1WJN"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:1WJN"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:1WJN"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:1WJN"
FT TURN 477..480
FT /evidence="ECO:0007829|PDB:1WJN"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:1WJN"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:1WJN"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:1WJN"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:1WJN"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:1WJN"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:1WJN"
SQ SEQUENCE 524 AA; 59086 MW; E95280086D80FEF8 CRC64;
MSDILPLDVI GRRVEVNGEY ATVRFCGAVP PVAGLWLGVE WDNPERGKHD GSHEGTMYFK
CRHPTGGSFV RPSKVNFGDD FLTALKKRYV LEDGPDDDEN SCSLKVGSKQ VQTIGFEHIT
KKQSQLRALQ DISLWNCAVS HAGEQGRIAE ACPNIRVVNL SKNLLSTWDE VVLIAEQLKD
LEALDLSENK LQFPSDSPTL TRTFSTLKTL VLNKTGITWT EVLHCAPSWP VLEELYLKSN
NISISERPVN VLQKMRLLDL SSNPSIDESQ LSLIADLPRL EHLVLSDIGL SSIHFPDAEI
GCKTSMFPAL KYLIVNDNQI SEWSFINELD KLQSLQALSC TRNPLSKADK AEEIIIAKIA
QLRTLNRCQI LPEERRGAEL DYRKAFGNEW RKAGGHPDPD KNRPNAAFLS AHPRYQLLCC
KYGAPEDEEL KTQQPFMLKK QLLTLKIKCS NQPERQILEK QLPDSMTVQK VKGLLSRLLK
VPVSELLLSY ESSKMPGREI ELENDLQPLQ FYSVENGDCL LVRW
